ID   PGCA_STAAN              Reviewed;         552 AA.
AC   Q7A3K7;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Phosphoglucomutase;
DE            Short=PGM;
DE            EC=5.4.2.2;
DE   AltName: Full=Alpha-phosphoglucomutase;
DE   AltName: Full=Glucose phosphomutase;
GN   Name=pgcA; OrderedLocusNames=SA2279;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the interconversion between glucose-6-phosphate and
CC       alpha-glucose-1-phosphate. This is the first step in the biosynthesis
CC       of diglucosyl-diacylglycerol (Glc2-DAG), i.e. the predominant
CC       glycolipid found in the S.aureus membrane, which is also used as a
CC       membrane anchor for lipoteichoic acid (LTA) (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB43582.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000018; BAB43582.1; ALT_INIT; Genomic_DNA.
DR   PIR; D90052; D90052.
DR   AlphaFoldDB; Q7A3K7; -.
DR   SMR; Q7A3K7; -.
DR   EnsemblBacteria; BAB43582; BAB43582; BAB43582.
DR   KEGG; sau:SA2279; -.
DR   HOGENOM; CLU_016950_0_0_9; -.
DR   UniPathway; UPA00894; -.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glucose metabolism; Isomerase; Magnesium;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN           1..552
FT                   /note="Phosphoglucomutase"
FT                   /id="PRO_0000308341"
FT   ACT_SITE        143
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  62359 MW;  37A8F8FFA0EF6976 CRC64;
     MKGCLATMDK ELWIERANDS LVKHFYEQQS DIEQREGFES KLTFGTAGIR GKFGLGEGRL
     NKFTIEKLAL GLARYLNAQT NSPTIVIHYD IRHLSTEFAQ IIANVLANHQ ITVYLPDTYK
     TTPELSFAVR NLNTTAGIMI TASHNPKDYN GIKVYGSDGA QLSTDASELA SRYIEEVGDP
     LQIDIPISKQ NTSYIKPFPK SVTDDYMKHI QNMIGYIPKS DLQVVFTSLH GTSVPIVPEL
     LKSLNFNQFN LVDAQCKPDP NFSSVQSANP EDHRAFDQAV ELANKSHADL LISTDPDADR
     LGIAERDAHG HITYFNGNQI GALLLNYRIQ QTSQLRHRLM IQSIVSSELT KSLARYNNVK
     YKEVLTGFKF IAQEIRQLDD HQNMIFAFEE SYGFLSEPFV RDKDAVQIVP LIIKYASELK
     LYGKTLKDEL EQIYQTVGRH EDTLFSHTLE GLEGKKKIES IMTHFRSNPP QEIQGLKVKA
     IEDYLTSEVY HLDKDTTSQI NSSKSNVIRV LFDEGFIALR PSGTEPKIKL YVSLKCPDFD
     DVAQKINAMI FS